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Solution structure of HI1506, a novel two-domain protein from Haemophilus influenzae.
- Source :
-
Protein science : a publication of the Protein Society [Protein Sci] 2007 May; Vol. 16 (5), pp. 977-82. Date of Electronic Publication: 2007 Mar 30. - Publication Year :
- 2007
-
Abstract
- HI1506 is a 128-residue hypothetical protein of unknown function from Haemophilus influenzae. It was originally annotated as a shorter 85-residue protein, but a more detailed sequence analysis conducted in our laboratory revealed that the full-length protein has an additional 43 residues on the C terminus, corresponding with a region initially ascribed to HI1507. As part of a larger effort to understand the functions of hypothetical proteins from Gram-negative bacteria, and H. influenzae in particular, we report here the three-dimensional solution NMR structure for the corrected full-length HI1506 protein. The structure consists of two well-defined domains, an alpha/beta 50-residue N-domain and a 3-alpha 32-residue C-domain, separated by an unstructured 30-residue linker. Both domains have positively charged surface patches and weak structural homology with folds that are associated with RNA binding, suggesting a possible functional role in binding distal nucleic acid sites.
- Subjects :
- Amino Acid Sequence
Bacterial Proteins genetics
Calorimetry, Differential Scanning
Haemophilus influenzae genetics
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Sequence Data
Protein Structure, Secondary
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Solutions
Bacterial Proteins chemistry
Haemophilus influenzae metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0961-8368
- Volume :
- 16
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Protein science : a publication of the Protein Society
- Publication Type :
- Academic Journal
- Accession number :
- 17400915
- Full Text :
- https://doi.org/10.1110/ps.072820907